Glucosidase, beta (Bile Acid) 2 (GBA2) ELISA Kits

Zebrafish Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

1. These results provide a foundation for the use of zebrafish in screening GBA2-targeting molecules, and for wider studies investigating GBA2 biology.

2. GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons.

Mouse (Murine) Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

1. results shed light on the molecular mechanism underlying the pathogenesis of GBA2-related hereditary spastic paraplegia (HSP), autosomal-recessive cerebellar ataxia (ARCA) and reveal species-specific differences in GBA2 function in vivo

2. sphingosine, the cytotoxic metabolite accumulating in Gaucher cells through the action of GBA2, directly binds to GBA2 and inhibits its activity.

3. GBA2 is particularly abundant in Purkinje cells (PCs), one of the most affected neuronal populations in NPC disease.

4. glucosylceramide accumulation in GBA2 knockout-mice alters cytoskeletal dynamics due to a more ordered lipid organization in the plasma membrane. Similar cytoskeletal defects were observed in male germ and Sertoli cells from GBA2 knockout-mice.

5. the deletion of Gba2 significantly rescues the type 1 Gaucher disease clinical phenotype.

6. redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin.

7. GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling.

8. The repression of IL-6/STAT3 signalling pathway seems to be one of the mechanisms for the delay of liver regeneration in GBA2-deficient mice.

9. GBA1 and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples.

10. The coiled-coil structure of LIMP-2 is required for its interaction with beta-glucocerebrosidase.

11. L-type calcium channel blockers have the ex vivo effects of increasing GCase activity and protein in mouse fibroblasts

12. GBA2 is a glucosylceramidase whose loss causes accumulation of glycolipids and an endoplasmic reticulum storage disease

13. the non-lysosomal glucosylceramidase is identical to the earlier described bile acid beta-glucosidase, being beta-glucosidase 2

14. testis GBA2 is present in both somatic and germ cells

Human Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

1. results shed light on the molecular mechanism underlying the pathogenesis of GBA2-related hereditary spastic paraplegia (HSP), autosomal-recessive cerebellar ataxia (ARCA) and reveal species-specific differences in GBA2 function in vivo

2. We conclude that the c.1780G>C mutation results in NLGase loss of function with abolishment of the enzymatic activity and accumulation of GlcCer accompanied by a compensatory increase in GCase.

3. Demonstrate that GBA2 plays a role in the proinflammatory state characterizing cystic fibrosis cells. Report for the first time that Pseudomonas aeruginosa infection causes a recruitment of plasma membrane-associated glycosphingolipid hydrolases into lipid rafts of CuFi-1-infected cells.

4. Our protocol showed high specificity and sensitivity for homozygosity detection and facilitated the identification of novel mutations in GAN, GBA2, and ZFYVE26 in four families affected by hereditary spastic paraplegia or Charcot-Marie-Tooth disease

5. GBA mutations as risk factors for PD and point to lysosomal dysfunction as a mechanism contributing to PD etiology.

6. GBA2 mutations causing a Marinesco-Sjogren-like syndrome in two Norwegian families, are reported.

7. Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2

8. sphingosine, the cytotoxic metabolite accumulating in Gaucher cells through the action of GBA2, directly binds to GBA2 and inhibits its activity.

9. The results suggested that SPG46 and SPG56 are rare causes of hereditary spastic paraplegia in China.

10. Spastic paraplegia/cerebellar ataxia patients have a severe deficit in GBA2 activity, because the GBA2 mutants are intrinsically inactive and/or reduced in amount.

11. SPG46 maps to 9p21.2-q21.12 in a Tunisian family with a complicated autosomal recessive hereditary spastic paraplegia with mental impairment and thin corpus callosum

12. The GBA2 gene shows a low mutation frequency in a general population of complicated hereditary spastic paraparesis

13. Whole-exome and targeted sequencing have defined the genetic basis of dizziness including new genes causing ataxia: GBA2, TGM6, ANO10 and SYT14

14. We hereby report a novel GBA2 mutation associated with spastic ataxia and suggest that GBA2 mutations may be a relatively frequent cause of autosomal recessive cerebellar ataxias.

15. observations make GBA2 a likely candidate to be involved in Gaucher disease etiology.

16. redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin.

17. GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons.

18. This study suggests GBA2 mutations are a cause of recessive spastic ataxia and responsible for a form of glucosylceramide storage disease in humans.

19. GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling.

20. GBA2 is down-regulated in melanoma; inducible expression of GBA2 affects endogenous sphingolipid metabolism by promoting glucosylceramide degradation (decrease by 78%) and ceramide generation.